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Heparanase: Breaking down barriers in tumors

Nature Medicine volume 5, pages 735–736 (1999)Cite this article

Abstract

Cloning and functional characterization of the long sought-after heparanase opens a new chapter in the understanding and potential manipulation of metastasis and inflammatory processes (pages 793–809).

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Figure 1: Possible roles of heparanase in inflammation and tumor invasion.

References

  1. Vlodavsky, I. et al. Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis. Nature Med. 5, 793–802 (1999).

    Article  CAS  Google Scholar 

  2. Hulett, M.D. et al. Cloning of mammalian heparanase: an essential enzyme involved in tumor invasion and metastasis. Nature Med. 5, 803–809 (1999).

    Article  CAS  Google Scholar 

  3. Chambers, A.F. & Matrisian, L.M. Changing views of the role of matrix metalloproteinases in metastasis J. Natl. Cancer Inst. 89, 1260–1270 (1997).

    Article  CAS  Google Scholar 

  4. Arribas, J. et al. Diverse cell surface protein ectodomains are shed by a system sensitive to metalloproteinase inhibitors. J. Biol. Chem. 271, 11376–11382 (1996).

    Article  CAS  Google Scholar 

  5. Nissen, N., Shankar, R., Gamelli, R., Singh, A. & DiPietro, L. Heparin and heparan sulphate protect basic fibroblast growth factor from non-enzymic glycosylation. Biochem. J. 338, 637–642 (1999).

    Article  CAS  Google Scholar 

  6. Freeman, C. & Parish, C.R. A rapid quantitative assay for the detection of mammalian heparanase activity. Biochem. J. 325, 229–237 (1997).

    Article  CAS  Google Scholar 

  7. Bame, K., Hassall, A., Sanderson, C., Venkatesan, I. & Sun, C. Partial purification of heparanase activities in Chinese hamster ovary cells: evidence for multiple intracellular heparanases. Biochem. J. 336, 191–200 (1998).

    Article  CAS  Google Scholar 

  8. Toyoshima, M., Dong, J., Kukula, A., Watanabe, T. & Nakajima, M. Purification and expression of human heparanase associated with tumor metastasis. Proc. Am. Assoc. Cancer Res. 40, 452 abstract 2988 (1999).

    Google Scholar 

  9. Kosir, M.A., Wang, W., Zukowski, K.L., Tromp, G. & Barber, J. Degradation of basement membrane by prostate tumor heparanase. J. Surg. Res. 81, 42–47 (1999).

    Article  CAS  Google Scholar 

  10. Vlodavsky, I. et al. Extracellular matrix-resident factors and enzymes: possible involvement in tumor metastasis and angiogenesis. Cancer Met. Rev. 9, 201–226 (1990).

    Article  Google Scholar 

  11. Schwartz, L.C. et al. Relationship between heparanase activity and increasing metastatic potential of fibroblasts transfected with various oncogenes. Cancer Lett. 51, 187–192 (1990).

    Article  Google Scholar 

  12. Mollinedo, F. et al. Major co-localization of the extracellular degradative enzymes heparanase and gelatinase in tertiary granules of human neutrophils. Biochem. J. 327, 917–923 (1997).

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Tumor Biology and Metastasis, Section of Cancer Therapeutics, Institute of Cancer Research, Cotswold Road, Sutton, SM2 5NG, Surrey, UK

    Suzanne A. Eccles

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  1. Suzanne A. Eccles
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Eccles, S. Heparanase: Breaking down barriers in tumors. Nat Med 5, 735–736 (1999). https://doi.org/10.1038/10455

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